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Results 1 - 10 of 14 > >>
EC Number Application Commentary Reference
Show all pathways known for 4.1.1.39Display the word mapDisplay the reaction diagram Show all sequences 4.1.1.39agriculture replacment of native wheat Rubisco with Hordeum vulgare enzyme increases photosynthetic performance at 25°C and at 35°C. At 25°C Rubisco from Hordeum vulgare maximally increases the assimilation rate by 22%. Exchange of residue K14Q is the only difference relative to Triticum aestivum cv Cadenza 748325
Show all pathways known for 4.1.1.39Display the word mapDisplay the reaction diagram Show all sequences 4.1.1.39agriculture replacment of native wheat Rubisco with the enzyme increases photosynthetic performance at 25°C and at 35°C. At 25°C Rubisco from Aegilops cylindrica maximally increases the assimilation rate by 23% 748325
Show all pathways known for 4.1.1.39Display the word mapDisplay the reaction diagram Show all sequences 4.1.1.39agriculture target for increasing agricultural productivity 649333
Show all pathways known for 4.1.1.39Display the word mapDisplay the reaction diagram Show all sequences 4.1.1.39analysis 1 pg of plant mRNA, ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit, is used to determine the efficiency of RT-PCR in general, and as a external reference gene for normalization of gene expression 694208
Show all pathways known for 4.1.1.39Display the word mapDisplay the reaction diagram Show all sequences 4.1.1.39analysis a method is established to remove ribulose bisphosphate carboxylase/oxygenase from plant samples to obtain high quality and high resolution 2D gels in proteome analysis 693851
Show all pathways known for 4.1.1.39Display the word mapDisplay the reaction diagram Show all sequences 4.1.1.39analysis a sensitive and robust mixed-mode high performance liquid chromatography-tandem mass spectrometry method is developed for the qualitative and quantitative determination of sugar phosphates 694678
Show all pathways known for 4.1.1.39Display the word mapDisplay the reaction diagram Show all sequences 4.1.1.39biofuel production engineered cyanobacteria with enhanced growth show increased ethanol production and higher biofuel to biomass ratio. Speeding up the Calvin-Benson-Bassham cycle theoretically has positive effects on the subsequent growth and/or the end metabolite(s) production. Four Calvin-Benson-Bassham cycle enzymes, ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO), fructose-1,6/sedoheptulose-1,7-bisphosphatase (FBP/SBPase), transketolase (TK) and aldolase (FBA) are selected to be cooverexpressed with the ethanol synthesis enzymes pyruvate decarboxylase (PDC) and alcohol dehydrogenase (ADH) in the cyanobacterium Synechocystis PCC 6803. An inducible promoter, PnrsB, is used to drive pyruvate decarboxylaseC and alcohol dehydrogenase expression. When PnrsB is induced and cells are cultivated at 0.065 mM photons/m*s, the RuBisCO-, FBP/SBPase-, TK-, and FBA-expressing strains produce 55%, 67%, 37% and 69% more ethanol and 7.7%, 15.1%, 8.8% and 10.1% more total biomass (the sum of dry cell weight and ethanol), respectively, compared to the strain only expressing the ethanol biosynthesis pathway. The ethanol to total biomass ratio is also increased in Calvin-Benson-Bassham cycle enzymes overexpressing strains. Using the cells with enhanced carbon fixation, when the product synthesis pathway is not the main bottleneck, can significantly increase the generation of a product (exemplified with ethanol), which acts as a carbon sink 748559
Show all pathways known for 4.1.1.39Display the word mapDisplay the reaction diagram Show all sequences 4.1.1.39biotechnology it is examined if recombinant protein accumulation can be enhanced by genetically fusing the recombinant reporter protein, luciferase, to the carboxy-terminal end of an abundant endogenous protein, the large subunit of ribulose bisphosphate carboxylase. A native protein-processing site from preferredoxin (preFd) is placed between the Rubisco LSU and luciferase coding regions in the fusion protein construct. Results demonstrate the utility of using fusion proteins to enhance recombinant protein accumulation in algal chloroplasts, and also show that engineered proteolytic processing sites can be used to liberate the exogenous protein from the endogenous fusion partner, allowing for the purification of the intended mature protein 702878
Show all pathways known for 4.1.1.39Display the word mapDisplay the reaction diagram Show all sequences 4.1.1.39biotechnology Rubisco appears as suitable objective for biotechnological optimization of hydrogen production because of its relevance controlling the hydrogenase main competitor electron sink (the Calvin-Benson cycle), as well as starch accumulation and photorespiratory oxygen consumption 716997
Show all pathways known for 4.1.1.39Display the word mapDisplay the reaction diagram Show all sequences 4.1.1.39biotechnology RuBisCO protein readily forms a network with a very high gel strength, but upon deformation it has a brittle character (low critical strain, low fracture strain). RuBisCO exhibits high potential as a functional ingredient for the design of new textures at low protein concentration 747998
Results 1 - 10 of 14 > >>